I have returned, but all this post will be is a random smattering of thoughts and excuses because that’s better than continuing to not update.

I have 4 drafts of half-written posts in which I try to tackle major topics or points of confusion, but (obviously) I haven’t posted any of them, even the ones I first started more than six months ago.

My most recent half-finished draft was abandoned when I realized 2 paragraphs in that it could easily be a book. The topic I was trying to address was human tissue use in research. I thought I could make a quick list of the major ethical concerns, another list of what types of human tissue are used in biology research, and then define each of those and address common misconceptions or at least explain the good, the bad, and the ugly and talk about what are historical versus modern practices. Why I thought that would all fit in a short blog post, I don’t know.

But I can tell you the inspiration for that post:

I made a mistake in my last post: the human cells I’m working with are not induced-puripotent stem cells (i.e. cells taken from adult, often skin cells from a cheek swab and reprogrammed into stem cells that are incapable of forming a human embryo but can still be differentiated into every cell type and used to study human cells), but they are actually an embryonic stem cell line. The specific line was made from WA09, a line created at the University of Wisconsin in 2001. Embryonic stem cell lines do actually come from embryos, but like the induced-pluripotent stem cells, we are not capable of making a human embryo from them. This particular line came from a medical center in Israel. The source of the tissue for embryonic stem cells is leftover tissue from IVF. When doing IVF, many more eggs are fertilized than will be needed to ensure there will be enough. Cells are taken from leftover blastocysts* a few days later.

*the first few paragraphs of that Wikipedia page will probably explain this better, but basically a blastocyst is a ball of cells that is the very early embryo.

Embryonic stem cells have some big advantages in that they are much more normal and mimic normal development much better than induced-pluripotent stem cells, making them far better for basic research applications. There certainly is more contention around their use, but I think it’s worth remembering that this tissue was taken from an abortion that would have been done anyway (I have never heard of a modern case of an abortion being done specifically to obtain cells, and if there is one, you’d be hard-pressed to find scientists who don’t agree that would be wildly unethical), and this single cell line has been around for 15 years and has been and will continue to give us a valuable model that has the advantage of 1) being human cells** and 2) not requiring sacrificing the comfort or lives of any people or animals to use.

**mice are really great for a lot of research, but they are not humans. This is one reason we’ve cured cancer in mice 100 different ways, but still struggle with treating it in people.

So what I’ve been up to the past few months is a lot of getting set up to grow and use the cells myself and continuing to work on both the photoreceptor project and my optogenetic project.

And to end the post, here’s a pretty picture of my photoreceptors! The green marks the photoreceptors and the purple binds the cytoskeleton (cyto=cell, skeleton; basically the structure that gives the cell its shape).

Note on edits: My original post mistakenly said that embryonic stem cells could come from abortions, which is entirely wrong. I think I’ve absorbed too much mainstream media and didn’t think critically enough about it. Fortunately another grad student corrected me, and once he said this it was really obvious why embryonic stem cells can’t possibly come from abortions: the cells need to be taken from a very, very early stage: a few days after fertilization and before implantation. Abortions happen weeks later and so they would never be a source of a cell line. All embryonic stem cell lines originally come from unused embryos from IVF (which would otherwise get frozen for later use, donated to another family for implantation, or destroyed). Sorry for spreading misinformation!

It turns out that one of the key tools for my project, the antibody against my protein, doesn’t work for me.

Quick refresher on antibodies: They are natural components of the immune system, huge proteins that have a region that can bind very specifically to molecules (such as proteins). Your body has somewhere between millions and billions of antibodies, each slightly different, and each able to bind to different things. In research we take advantage of this to purify antibodies that very specifically bind to just the protein we’re interested in. This is done by injecting large amounts of your protein of interest into an animal such as a rabbit, mouse, or goat, then letting their immune systems make tons of antibodies against that, then drawing their blood and purifying the antibodies.

Ideally you can inject whole, purified protein (you can oftentimes have E. coli make a bunch of your protein using molecular biology techniques). But because my protein of interest is imbedded in the membrane, it’s much harder to get E. coli to make it, and it’s much harder to purify. So instead the antibody was raised against a small bit of the sequence. So the idea is that the antibody will bind to the ~12 amino acids* of my protein of interest.

*If a protein is a balled up necklace, the amino acids are the beads; they are the protein building blocks.

But my antibody seemed to bind to many other things. So I did some googling (okay, slightly more sophisticated than googling, but I used online search tools to search for that 12 amino acid sequence in all the proteins in Xenopus leavis (the frogs we use). It turns out I got a few hits, so it was likely that my antibody does bind to things other than my protein of interest. Which basically would make all my data messier and possibly unusable.

But the real nail in the coffin came when I decided to look at where exactly the antibody was binding within the sequence in my protein. And I discovered that the answer is…. nowhere.

The sequence used to make the antibody came from Xenopus tropicalis, a close relative of X. laevis. And while their protein sequences are very similar, they’re not identical. It turns out the regions chosen to make the antibody against was almost completely different. So now I have an antibody that binds many things, but does not bind the protein I actually need it to bind.

And there isn’t really anyone to blame. The X. laevis genome wasn’t even sequenced until 2010, and no versions of it were widely available until 2012, and my understanding is that even the most current version has some issues**. So it’s pretty common to use X. tropicalis sequences as a starting point for X. laevis work. This is because tropicalis has a much easier to work with genome. Tropicalis is diploid, meaning it has two copies of each chromosome (one from mom, one from dad; the same as humans). But laevis are tetraploid, meaning they have four copies of each chromosome. This basically just makes the sequence a little messier and harder to identify any give base pair as “correct”, a normal variation (such as a different allele), or an abnormal variation (such as a mutation).

**it’s actually entirely possible that the sequence I’ve used to determine the antibody doesn’t bind is actually itself incorrect, but the fact that the antibody binds to so many other things makes it pretty useless to me anyway.

The moral of the story is that I have a new project! Since I’m late enough with this post as is and because I’m still in early planning and thinking and reading stages anyway, I’ll wait to tell you details until next week. But the basic project is retina regeneration! I’ll be using human induced-pluripotent stem cells that have been differentiated into retinal cell types, and I’ll be studying what helps or hurts their growth and what influences their axon pathfinding.

Also I’ll talk briefly about about human induced-pluripotent stem cells (a.k.a. iPSC). These are cells taken from adults (usually skin cells, such as from a cheek swab) that are essentially deprogrammed through environmental and sometimes genetic manipulations in order to turn them into a stem cell, a cell capable of becoming almost any cell. These cells can’t make a whole organism. They’re pluripotent (capable of making many different cell types) but they are not totipotent (capable of making all cell types). While they’re not the same as looking at actual development (which is where model organisms like xenopus and mouse really come in handy), human iPSCs are a great way to see if the things we discover in animal models hold true for human cells as well without, you know, actually experimenting on people. And the project I’ll be working on is within the context of stem cell-generated replacement retinas that could be implanted in patients with damage or disease to hopefully restore functional sight. So in this context, we actually want to understand how human iPSCs behave themselves (though the things we learn will definitely be more broadly applicable to development, regeneration, and human cell biology).

So I have some pretty exciting stuff to look forward to! Failure’s not all bad. And having heard some other stories, I’m pretty happy it only took 6 months, rather than several years, to figure out my previous project wasn’t going to work. And maybe in a few years when I have a firm foundation with this project, I can look into some new tools and pick up the other one again.

I almost forgot to post this week! I’m finally making progress on my first project (the morpholino one) which means I have time to work on the second one (the optogenetics one)! While it’s technically possible to work on both simultaneously, they both require a lot of the same first steps (injecting embryos, dissecting spinal cords), and I don’t yet trust myself to have the mental dividers to not mix them up, haha.

All this progress means I have more to do, which means I’ve been in lab a lot more the past two weeks (and still smooshing in small dance trips on the weekends). This is probably true in other fields as well, but certainly in science, progress seems to be exponential. Because once something works, even just a little bit, there are 5 ways you could verify it and 10 follow-up questions and 1,000 variations on the original experiment, all of which would be valuable to some degree.

Oh, but I have one thing I meant to post about a couple weeks ago and can talk about now: summer internships.

I was recently asked how valuable I thought my summer internship was (I did the Summer Undergraduate Research Fellowship at Mayo Graduate School the summer before my senior year) in terms of preparing me for grad school. My immediate response was, “A million*.” Which is to say that internship 1) is the reason I realized I wanted to go to grad school, 2) showed me what actually doing biological science was like day-to-day, and 3) was what changed my focus from behavioral neuroscience to cell biology. Basically without this internship, I’m quite sure I wouldn’t be in a cell biology program. Not just because they wouldn’t have let me in (undergrads who want to go to grad school in the sciences: research experience is a prerequisite for grad school these days; but also know that being a lab technician for a few years totally counts, so you don’t necessarily need to get that experience during undergrad; it’s never too late to go to grad school and your current state will not lock you into any one thing!), but also because I just wouldn’t have realized that cell biology was what I was really interested in and so at best I would have ended up in a program I didn’t like as much.

I also think that my internship was extra valuable because my project really was my own. This is often not true of undergraduate research opportunities (some other people doing the same program basically just did what their grad student told them to do). I basically got lucky. I was working with a grad student, but my project wasn’t just supporting his. This meant that I was expected to plan experiments myself and do them all myself. Which threw me off the first week or two (I spent a bit waiting for someone to tell me what to do because that’s what my lab experience up to that point had been**). But once I realized it was up to me to read the literature and make decisions about dosages and experimental design, I got going and learned a ton. I also had some excellent advice from my PI that helped set the tone for the summer: ask a question during every talk you go to. Because that forces you to 1) pay attention so you can come up with a good question (harder than you might think at 4pm with the lights off) and 2) think about what information you’re missing. And it may be a question about their methods in order to personally verify that their conclusions make sense, or it may be a question about the next directions and the broader context of the work. And both of these are super important questions to ask about other people’s work because it helps your understanding and gives you practice so you can ask those questions well about your own work.

At the end of the summer, there was a poster session where all the undergrads presented their work. Most people had fancy looking posters that they had gotten printed up by printing services, and they had pretty pictures and fancy coloring schemes. I printed out powerpoint slides on normal paper (a suggestion from a grad student) because I was still collecting and analyzing data the day before the poster session, so I had to be able to add or take away information as it changed or got updated.

So I have these 8.5×11 sheets pinned up to the board, and while they looked nice and had a cohesive color scheme, they didn’t look nearly as fancy as anyone else’s. But one person gave me my favorite (admittedly passive aggressive and slightly backhanded) compliment, “It looks like you actually did the work for your poster!”

Moral of the story: research experience is absolutely essential for grad school, but I also highly recommend seeking out (or creating) opportunities where you are in charge of your project.

*I was looking for a way to say “a lot” but even more emphatically, and this was the phrase my brain chose.
**During my junior year, I did research in a psych lab with human participants. While it was a really valuable experience in terms of teaching me about hypotheses and proper experimental design, I was literally working off a script (to make sure the interaction with each participant is as similar as possible) and I jumped in partway through years worth of data collection, so I had no direct role in the actual planning of the experiment. And lab courses were always just “Do X, Y, and Z in this order.”

I have data! Finally! Right now the question I’ve answered is pretty preliminary: where is my protein located in normal cells? And here’s a pretty picture (unusable for data analysis or publication unfortunately due to some missing information, but pretty nonetheless):

This is a frog growth cone (the growth cone is the part of the developing neuron at the end of the growing axon). The green is my protein. The purple is actin, which is a component of the cytoskeleton (the cytoskeleton is basically the structural scaffold of the cell, giving it shape and the rigidity necessary for directed movement).

And the answer to where my protein is located is that it’s not exactly where we expected it to be (though it’s not super weird either). Basically it seems to be concentrated in the axon (see the bright green line in the top left? That’s an axon), which is where the major protein highway of the neuron is located: microtubules. Neurons have a cell body (where the DNA is located and where most proteins are made) and a very long (relative to their size) axon that extends out. To send proteins down to the end of the axon, the proteins are attached to motor proteins with little feet that basically walk them down the microtubule highway (microtubules are basically what they sound like: small tubes). So seeing a ton of our protein in the axon suggests that it’s probably being moved via this highway system. Which is cool! Figuring out how a cell decides how much of a protein it needs where (and how the cell actually accomplishes it) can be just as interesting as figuring out what the protein actually does once it’s there.

And this evening I’ll finally (hopefully) get data with my morpholino experiments. Those will answer the question of “what happens when neurons don’t have much of this protein?” Asking this type of question and taking this approach is called a loss of function experiment. And there are basically only 3 types of experiments:

1) Observation: What happens under normal conditions? Where is the thing located? When is it there? What is it doing? That last one may or may not be answerable with observation alone, especially not in molecular biology. The experiment I got data on was observational; I just looked at where my protein was under normal conditions.
2) Loss of function: What happens when this thing is gone or broken? This includes things like gene knockouts, morpholinos, and drug inhibitors. They are how you can determine necessity: is this thing necessary for a given process or outcome to occur?
3) Gain of function: What happens when you have extra of this thing, or have this thing where/when it isn’t normally there? This is how you determine sufficiency: is this thing sufficient to cause a given process or outcome? This is often accomplished by inducing overexpression of a protein (if you inject in extra DNA or RNA, the protein will make extra) or by breaking something that prevents the protein from working (removing the inhibitor should increase the activity).

So I have an observational experiment done, and I’m about to get data on a loss of function experiment. I actually don’t have a specific gain of function experiment planned right now (though I know of at least one thing that’s inhibiting my protein, so I could remove that). Actually my next steps are probably going to be observational: what is my protein interacting with? There are a few ways I can do that. One simple method is by staining and seeing what’s in the same place as my protein. Another approach is looking for functional association: if I break two things at the same time and they cause a change that is less than the sum of breaking each of them individually, it suggests that they may be interacting or part of the same pathway. To explain that another way:

If A activates B in order to cause C, breaking either A or B would cause C to not happen. And breaking both A or B would also cause C to not happen. However if A and B caused C independently from one another, breaking either of them would cause a decrease in C but would not get rid of C entirely. However breaking both A and B would still cause C to stop completely. And you can use that logic to construct experiments to determine if A and B are in the same or separate pathways.

So that’s what I’ve been up to! It’s definitely exciting finally having data to analyze. I get to make pretty graphs! And I actually really like data crunching days; it can be really relaxing to not worry about timers going off or making sure I regulate my caffeine intake enough to avoid shaky hands during dissections. Instead I can just hang out at the computer, drink coffee, and listen to music and I measure and play around with images and graphs. And then seeing my data graphed and being able to visualize my results is the most exciting part! And that gives me a jumping off point to hypothesize about what might be causing the results and what might actually be happening, which is easily one of my favorite parts of science. Yay for data and data interpretation!

I made RNA, made DNA, and verified that I can stain extracellularly with my antibody!

Which sounds like gibberish (or near gibberish), so here’s the breakdown:

Making RNAI’ve mentioned before that one big advantages to using Xenopus laevis (frog) embryos for developmental research is that the eggs are huge, so we can inject them with things.
Here’s an image (just pulled from google) to show that. On the left you can see a glass tube, which is actually a needle. We use a machine that heats up the glass tube and pulls it to be a certain diameter. You can then stick that (using a device called a micromanipulator that holds the needle for you and can be moved along multiple axes by turning dials).

And my current main experiment involves injecting a morpholino (which is a man-made chemical similar to DNA or RNA). But you can also just inject DNA or RNA.

Quick reminder that DNA is transcribed to make RNA, and then the RNA is translated into protein. And the proteins are what actually do all* the stuff in your cells.

*Well, they don’t do everything. RNA actually can do some things, but proteins are the bulk of the actors. They modify molecules and other proteins, move molecules and other proteins, and bring together molecules and proteins in specific patterns.

So if you inject DNA or RNA, the cell will actually work with it and make stuff from it. So if you inject DNA, it will make RNA from it, and then make protein from that RNA. And if you inject RNA, it will make protein straight from that.

There are some advantages to injecting RNA instead of DNA (basically you get more cells actually making the protein), so I wanted to make some RNA that will encode a red fluorescent protein called mCherry.

Okay, I started explaining how exactly I did that, but quickly realized that to really explain it would mean explaining a lot of background concepts, and it’s Friday afternoon, so I want to go hang out with people instead of sitting here writing about molecular biology for several hours, haha. But basically you can put your DNA, RNA nucleotides (basically RNA legos), and the proteins that can put together the RNA legos to build an RNA strand based on the DNA all together in a test tube, let it sit for several hours at 37°C and magic happens! And then you purify out the RNA.

The real trick with making RNA is that your body actively destroys RNA. You secrete a protein called RNase. RNase chops up any RNA it encounters. And your skin cells, hair, sweat, tears, mucus, saliva etc all have a ton of this stuff. Which means if I breath too hard on my RNA, it could all get degraded! So I have to be very careful (no talking, clean the whole bench down with a spray called RNase-Away, use gloves and change them after touching anything else).

But I succeeded! And now I have some mCherry RNA to play with (and by “play”, I mean “use for important experiments”).

Making DNAAgain I’m not gonna actually explain too much (sorry!), but basically I didn’t have enough of another DNA and wanted more of it. In biology we use E. coli to help us out in these situations! E. coli will take up DNA from their environment under the right conditions (which we can easily create in the lab). So I just had to get them to take up my DNA, grow them up in some bacteria-friendly, nutrient rich liquid, and then purify out my DNA.

So I’ll explain a bit about how I get the DNA I want and not a bunch of E. coli DNA, because that’s pretty cool. Basically, the DNA I want is in a little circle of DNA called a plasmid. Bacteria typically have lots of plasmids (which is actually how they can easily acquire resistance to antibiotics – they can trade plasmids with other bacteria, so if they meet and mate with a cell that has developed antibiotic-resistance, it can acquire the trait by taking up those antibiotic-resistance genes). But the ones I’m using do not. And the rest of the E. coli genome is on a much larger strand of DNA (called genomic DNA because, well, it’s the stuff that’s actually in the genome rather than these extra plasmids. In the picture below it’s labeled “Bacterial DNA”).

After I’ve grown up a bunch of bacteria that have my plasmids in it, I lyse the cells. Lysing is basically breaking them apart, so I disrupt their outer membrane so all the DNA is now just in solution in my tube (along with everything else). To separate my plasmid DNA from the genomic DNA, I take advantage of the fact that my plasmids are little and the genomic DNA is much larger. I can put my tubes in a centrifuge, which basically spins them incredibly fast (13,000 rotations per minute), which separates everything based on size (the biggest things go to the bottom). So now all the big genomic DNA is at the bottom, while my plasmid is at the top. So I can pull off the solution that has my plasmid in it and purify it from there. (The purification at that point involves a filter that the DNA binds to).

Antibody Stuff
I’ve talked about antibody staining before. But basically I can use an antibody that binds to my protein of interest to label it. I add on the antibody and it binds to all my protein, and then I add a fluorescent antibody that binds to that first antibody. And normally when we do this in fixed tissue (fixed meaning preserved, like formaldehyde) we put the cells in a solution that causes the outer membrane to become porous, so the big antibodies can get through. But I wanted to see what of my protein was imbedded only on the outer membrane, and not what is actually inside the cell. Fortunately, the part of my protein that my antibody binds to is a bit that sticks out on the surface of the cell. So in theory I could skip the step where we permeabilize that outer membrane, so none of the antibody would get inside the cell, and I could see only what bound to my protein on the outside.In theory it would work, but I wanted to actually try it out before incorporating it into my experiment (just because I don’t want to do a ton of work just to find out my detection method is faulty). And it does work! Unfortunately I had some technical issues (i.e. I destroyed almost all the cells from two of my three slides), so I’ll certainly be repeating the experiment. But at least I know it’s something I can do, so I can rely on that in the future if I want to!

So that’s been my week! And I’m all done with classes for the year, so I’m suddenly so much more productive in lab. Which is awesome because that’s what I actually want to be doing. While classes are certainly valuable, I’m just ready to be done. And I’ve finished all the classes required for my program (yay for being in a program with low class requirements!). That doesn’t necessarily mean I won’t have any more to take (my thesis committee will decide that when I meet with them in August), but at least it will probably only be one or two more, so I’ll almost certainly no longer have class every day of the week.

I’ve started reading the blog Serial Mentor by a PI at University of Texas Austin, and he’s got some awesome (though much more science- and academia-specific posts than most of you probably care about). But he has a great post about the problems with academic-style writing and how to improve your writing.

And having just written a final paper and final exam for classes, it was really obvious how much I’ve ingrained a lot of the “correct” scientific writing practices that are actually terrible. Actually when I was writing my exam, I realized I had a sentence that really should have been about 4 sentences. I ended up crossing it out and restarting because it was so unweildy I couldn’t end it. And I am the master of sentences so long that they seem like they’re run-ons even though technically they’re not, haha.

But I’ve also been thinking about how scientific language is an impediment to public understanding. I remember in undergrad, reading a scientific paper was really difficult. And part of it is that there are a lot of terms you don’t know, and the more you get used to hearing certain words, the easier it gets. But the sentence structure that’s common is also incredibly difficult to understand. Usually there are prepositional phrases on prepositional phrases, so it’s hard to figure out what’s actually happening (as serial mentor’s post points out).

Which is funny because the goal of scientific writing is supposed to be clarity. That’s the reason it should be different from literary writing: you want to get to the point clearly and concisely. But that’s not at all what actually happens when you use passive voice and prepositional phrases for days.

Another thing I’ve been thinking about related to science writing and communication: in science we tend to be really careful about our word choice. There are very few things we can say with any certainty, so we carefully hedge our sentences to be clear that “the evidence suggests” or “these findings would indicate” and avoid saying “this is the way it is” because you can never prove anything with 100% certainty. Additionally, we often use highly specific terms because even small variations in the way an experiment is done can make a big difference.

But while these differences are very important in a research context, they’re pretty useless for explaining to the general public. The general public doesn’t care about details, and including them can make things more confusing than it’s worth. I think that sometimes explaining things a little bit wrong is better than being technically correct but having nobody understand.

So I’ve been trying to incorporate a great improv technique into my explaining: “yes and.” For those who haven’t done improv before, the idea of “yes and” is that you never shoot down somebody’s idea, because it shuts everything down and makes for terrible comedy. For instance:

“I’m an elephant! *flails arm-trunk*”
“Yes, and we’re on our way to Pride Rock to meet Simba!”

And I think this technique is also super valuable for explaining complicated concepts, and I’m trying to be better at incorporating it in my explanations (as well as the rest of my life). For instance when I took physics, I had what I thought was a very logical realization: because electrical currents generate magnetic fields, what made magnetic objects magnetic was that the electrons moved around atoms in a synchronous way that generated a magnetic field. And when I asked the TA about it, his response was basically “Well, not really, but you haven’t taken enough math for me to be able to explain it to you.” Which just left me more confused. And what I think would have been more valuable would have been him saying, “Yeah, that’s a good way to think about it! And here’s this extra piece of knowledge to build off of that.” In that second version, I would have learned something new from the interaction instead of just feeling like physics was a confusing and impenetrable subject.

So I want to be better at saying “yes and” as well as writing and communicating in ways that are clear, instead of just trying to be technically correct or sound official.

Two weeks ago I talked about how I’ve actively chosen to not to live and breathe only grad school (and actually I forgot to do a post last week because I was at a dance convention). But obviously I’m here. And this is absolutely where I want to be. So today I’m gonna talk about why.

First: I’m a question-asker. I have been given multiple nicknames based on how many questions I ask. From several completely distinct groups of people. I ask a lot of hows and whys. Which pretty clearly lends itself to scientific research. I just really like figuring out how things work.

Second: I’m a learner. I’ve always been that kid who enjoyed classes (yes, I even enjoyed high school). I love learning new things, and much of my free time is spent doing just that: I have historically jumped from hobby to hobby fairly often, and I think a lot of that is that I like picking up new things because there’s so much to learn when you start something new (For instance I’ve taken lessons in 7 instruments and mastered exactly none of them). So to basically get to spend 5 years being paid to learn about things I find really interesting and important? Pretty good deal.

Third: I’m a problem solver. I love puzzles. I love logic puzzles, I love crosswords, I even love 5000 piece puzzles of lighthouses. And solving research problems is like all of those things times a million. It’s like having a 5000 piece puzzle where you have to critically analyze each piece to make sure it even belongs in the puzzle and that the manufacturer didn’t accidentally make it the wrong shape. And other people have put together the top left corner, so you have to find that so you don’t redo that whole section that’s already known. And you may have a vague idea of what you think the picture will be of, but you may be entirely incorrect. Which would be an incredibly frustrating puzzle and would probably sell terribly. But while research is absolutely frustrating (guess who gets to redo two thirds of what they did this week because it didn’t work??? me!!!), I can get bored easily, so having a difficult problem with twists and turns is pretty much perfect for me.

Fourth: I’m a crafter. I actually love the physical actions of doing cell biology research. I like dissecting and I like pipetting. I knit and sew, both of which involve lots of careful planning followed by lots of repetitive, somewhat tedious actions. Which I actually really enjoy. The simple physical actions can be a nice break from the creative problem solving. And the more difficult ones (I keep getting too many muscle cells in my spinal cord dissections) are something I can practice at to get better.

Basically grad school (and cell biology research more generally) incorporates a lot of aspects that really appeal to me. I have yet to hear about a career path that does that as well (while I occasionally daydream about being a woodworker or pattern drafter or dance teacher, they all have 1-3 things I’d love and 20+ things I’d hate). So even though I don’t want it to be 100% of my life, I really love that it’s a large chunk of it.

Also sorry this sounds like a grad school application/interview, haha. It’s hard to talk about why I like grad school without it sounding really cheesy. Also I will say that even though I realized during undergrad that I would enjoy grad school, I didn’t decide to actually apply until I thought more about what career I wanted and whether I needed grad school to get me there. And I eventually realized that I wanted a career where I could be doing the project planning and critical thinking and literature analysis, and that meant I needed a PhD.